Abstract
Rac1 (Ras-related C3 botulinum toxin substrate 1) protein has been found in the cell nucleus many years ago, however, its nuclear functions are still poorly characterized but some data suggest its nuclear accumulation in cancers. We investigated nuclear Rac1 in glioma cancer cells nuclei and compared its levels and activity to normal astrocytes, and also characterized the studied cells on various nuclear properties and cell migration patterns.Nuclear Rac1 indeed was found accumulated in glioma cells, but only a small percentage of the protein was in active, GTP-bound state in comparison to healthy control. Altering the nuclear activity of Rac1 influenced chromatin architecture and cell motility in GTP-dependent and independent manner. This suggests that the landscape of Rac1 nuclear interactions might be as complicated and wide as its well-known, non-nuclear signaling.
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